Intracellular Ca
2+ plays important roles in versatile cellular functions. Incerease in the intracellular Ca
2+ concentration via either Ca
2+ influx from the extracellular space or Ca
2+ mobilization from the intracellular Ca
2+ store sites causes Ca
2+ binding to its intracellular receptor, Ca
2+-binding proteins. Many Ca
2+-binding proteins are found and their functions have been partly elucidated. In this article, I would like to introduce the recent progress in the molecular mechanisms by which the Ca
2+ signal is mediated in the cell. Especially, molecular characteristics of calmodulin, the most characterized Ca
2+- binding protein, are detailed. Furthermore, this paper describes calmodulin-dependent protein kinases as the main target proteins of calmodulin, and kinas cascade composed of these kinases and newly found CaM kinase kinase. Finally, pharmacological approaches using specific inhibitors of the CaM kinase family are discussed.
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